ID   PLIA_BOTER              Reviewed;         166 AA.
AC   B1A4N2; B1A4N3;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 42.
DE   RecName: Full=Phospholipase A2 inhibitor;
DE            Short=alpha-PLI;
DE   Flags: Precursor;
OS   Bothrops erythromelas (Caatinga lance head).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX   NCBI_TaxID=44710;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RA   Estevao-Costa M.I., Costa M.A.F., Mudado M.A., Franco G.R.,
RA   Fortes-Dias C.L.;
RT   "A profile of the phospholipase A2 inhibitors of the alpha class prospected
RT   in Brazilian Crotalidae snakes: structural and phylogenetic analysis.";
RL   Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This phospholipase A2 inhibitor binds directly phospholipase
CC       A2 in the presence or absence of calcium. {ECO:0000250}.
CC   -!- SUBUNIT: Homotrimer; non-covalently linked.
CC       {ECO:0000250|UniProtKB:A1XRN2}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|Ref.1}. Note=Secreted in
CC       plasma. {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed by the liver. {ECO:0000305|Ref.1}.
CC   -!- SIMILARITY: Belongs to the alpha-type phospholipase A2 inhibitor
CC       family. {ECO:0000305}.
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DR   EMBL; EU421906; ABZ82323.1; -; mRNA.
DR   EMBL; EU421907; ABZ82324.1; -; mRNA.
DR   EMBL; EU421908; ABZ82325.1; -; mRNA.
DR   EMBL; EU421909; ABZ82326.1; -; mRNA.
DR   EMBL; EU421910; ABZ82327.1; -; mRNA.
DR   EMBL; EU421911; ABZ82328.1; -; mRNA.
DR   AlphaFoldDB; B1A4N2; -.
DR   SMR; B1A4N2; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0019834; F:phospholipase A2 inhibitor activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.100.10; -; 1.
DR   InterPro; IPR001304; C-type_lectin-like.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR018378; C-type_lectin_CS.
DR   InterPro; IPR016187; CTDL_fold.
DR   Pfam; PF00059; Lectin_C; 1.
DR   SUPFAM; SSF56436; SSF56436; 1.
DR   PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Disulfide bond; Glycoprotein; Lectin; Phospholipase A2 inhibitor;
KW   Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000250"
FT   CHAIN           20..166
FT                   /note="Phospholipase A2 inhibitor"
FT                   /id="PRO_0000355229"
FT   DOMAIN          46..161
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   CARBOHYD        61
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        122
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        83..160
FT                   /evidence="ECO:0000250|UniProtKB:P21755"
FT   DISULFID        138..152
FT                   /evidence="ECO:0000250|UniProtKB:P21755"
FT   CONFLICT        43
FT                   /note="F -> V (in Ref. 1; ABZ82324)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   166 AA;  18375 MW;  97768E127C55BDEB CRC64;
     MRLILLSGLL LLGIFLANGH EQDPDGKVLN SLIDALMHLQ REFAKLRGAF LTVYKARSFG
     NGSERLYVTN KEIKNFEALR QICEQAGGHI PSPQLENQNK AFANVLERHN KEAFLVVGDS
     ANFTNWAAGQ PNKAAGTCVK ADTHGSWHSA SCDDNLLVVC EFYFIL